ID A0A248KJ49_9ENTR Unreviewed; 451 AA.
AC A0A248KJ49; A0A6G9RNT4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:ASG63614.1};
GN ORFNames=CEW81_14790 {ECO:0000313|EMBL:ASG63614.1}, GY169_14520
GN {ECO:0000313|EMBL:QIR27943.1};
OS Kluyvera genomosp. 3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kluyvera.
OX NCBI_TaxID=2774055 {ECO:0000313|EMBL:ASG63614.1, ECO:0000313|Proteomes:UP000197098};
RN [1] {ECO:0000313|EMBL:ASG63614.1, ECO:0000313|Proteomes:UP000197098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YDC799 {ECO:0000313|EMBL:ASG63614.1,
RC ECO:0000313|Proteomes:UP000197098};
RA Ito R., Pacey M.P., Doi Y.;
RT "Origin of plasmid-mediated fosfomycin resistance gene fosA3.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QIR27943.1, ECO:0000313|Proteomes:UP000503580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PO2S7 {ECO:0000313|EMBL:QIR27943.1,
RC ECO:0000313|Proteomes:UP000503580};
RA Singha K.M.;
RT "Whole genome PO2S7.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|RuleBase:RU361152};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR EMBL; CP022114; ASG63614.1; -; Genomic_DNA.
DR EMBL; CP050321; QIR27943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248KJ49; -.
DR KEGG; kgo:CEW81_14790; -.
DR Proteomes; UP000197098; Chromosome.
DR Proteomes; UP000503580; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR InterPro; IPR019802; GlycHydrolase_4_CS.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR022616; Glyco_hydro_4_C.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW NAD {ECO:0000256|RuleBase:RU361152};
KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000197098}.
FT DOMAIN 198..421
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 113
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 451 AA; 50479 MW; A0CA7D53656C25C7 CRC64;
MMTAPKITFI GAGSTIFVKN ILGDVFHREA LKSAHIALMD IDATRLEESH IVVRKLMDSA
GASGHITCHT DQRAALQGAD FVVVAFQIGG YEPCTVTDFE VCKRHGLEQT IADTLGPGGI
MRALRTIPHL WQICEDMSEL CPNATMLNYV NPMAMNTWAM YARYPHIKQV GLCHSVQGTA
EELARDLGID PASLRYRCAG INHMAFYLEL ERKNADGEYV NLYPELLAAY AAGEAPKPNI
HGNTRCQNIV RYEMFKKLGY FVTESSEHFA EYTPWFIKPG REDLIERYKV PLDEYPKRCV
EQLANWHKEL EEYKTAERID IKPSREYAST IMNALWTGEP SVIYGNVRND GLIDNLPQGS
CVEVACLVDA NGIQPTKVGA IPAHLAAMMQ TNINVQTLLT EAILTENRDR VYHAAMMDPH
TAAVLGIDEI YALVDDLITA HGDWLPAWLH R
//
